M
Mary L. Westbrook
Researcher at Argonne National Laboratory
Publications - 14
Citations - 832
Mary L. Westbrook is an academic researcher from Argonne National Laboratory. The author has contributed to research in topics: Detector & Detective quantum efficiency. The author has an hindex of 7, co-authored 14 publications receiving 811 citations.
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Journal ArticleDOI
The three-dimensional crystal structure of cholera toxin.
Rong-Guang Zhang,David Scott,Mary L. Westbrook,Sharon Nance,Brenda D. Spangler,G. Graham Shipley,Edwin M. Westbrook +6 more
TL;DR: The three-dimensional structure of choleragen, along with those of related toxins from Shigella dysenteria and Bordetella pertussis, offer a first step towards the rational design of new vaccines and anti-microbial agents.
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Structure of the hirugen and hirulog 1 complexes of alpha-thrombin.
Ewa Skrzypczak-Jankun,Vasili E. Carperos,K. G. Ravichandran,Alexander Tulinsky,Mary L. Westbrook,John M. Maraganore +5 more
TL;DR: The isomorphous structures of the hirugen (N-acetylhirudin 53′-64′ with sulfato-Tyr63′) and hirulog 1 (d -Phe-Pro-Arg-Pro-(Gly)4 desulfato-tyr 63′-hirugen) complexes of human α-thrombin have been determined and refined at 2.2Aresolution to crystallographic R-factors of 0.167 and 0.163, respectively as discussed by the authors.
Journal ArticleDOI
The 2.4 Å Crystal Structure of Cholera Toxin B Subunit Pentamer: Choleragenoid
R. Zhang,Mary L. Westbrook,Edwin M. Westbrook,Edwin M. Westbrook,David Scott,Zbyszek Otwinowski,P R Maulik,Robert A. Reed,G. Graham Shipley,G. Graham Shipley +9 more
TL;DR: The structure of the B subunits, and their pentameric arrangement, closely resembles that reported for the intact holotoxin, choleragen, the heat-labile enterotoxin from Escherichia coli, and for a Choleragenoid-GM1 pentasaccharide complex.
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Ccd-Based Detector for Protein Crystallography with Synchrotron X-Rays
M. G. Strauss,Edwin M. Westbrook,Istvan Naday,T.A. Coleman,Mary L. Westbrook,Dale J. Travis,Robert M. Sweet,James W. Pflugrath,Martin Stanton +8 more
TL;DR: In this paper, a detector with a 114 mm aperture, based on a charge-coupled device (CCD), has been designed for X-ray diffraction studies in protein crystallography.
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Characterization and data collection on a direct-coupled CCD X-ray detector
Istvan Naday,Edwin M. Westbrook,Mary L. Westbrook,Dale J. Travis,Martin Stanton,Walter Charles Phillips,Daniel M. O'Mara,Juanhui Xie +7 more
TL;DR: In this paper, a large area, multi-module, CCD-based detector without intensification stages is developed for X-ray diffraction applications, which consists of a fiberoptic taper with a phosphor deposited on the large end and a large format, scientific CCD bonded to the small end.